Isolation of a tumor cell laminin receptor

Rao, N C; Barsky, Sanford H.; Terranova, Victor P.; Liotta, Lance A.

doi:10.1016/0006-291x(83)91370-0

Cited by 393 publications

(197 citation statements)

References 9 publications

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“…One of these isoforms, the 67 kDa high affinity laminin receptor (LR: presumably the mature form of the receptor), is thought to arise from the heterodimerization of its precursor molecule, the 37 kDa LRP, with a still unidentified molecule (Buto et al, 1998). The 67 kDa LR is believed to be the functional isoform of the receptor regarding its ability to mediate strong attachement of cells to laminin (Lesot et al, 1983;Malinoff and Wicha, 1983;Rao et al, 1983), to be overexpressed on cancer cell sufaces, and to promote the invasive and metastatic capacity of these cells (Menard et al, 1997). Thus, it is of crucial importance to investigate whether this isoform is normally expressed in mouse brain and whether this isoform binds PrP.…”

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confidence: 99%

Different Isoforms of the Non-Integrin Laminin Receptor Are Present in Mouse Brain and Bind PrP

Simoneau¹,

Haı̈k²,

Leucht³

et al. 2003

Biological Chemistry

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confidence: 99%

Different Isoforms of the Non-Integrin Laminin Receptor Are Present in Mouse Brain and Bind PrP

Simoneau¹,

Haı̈k²,

Leucht³

et al. 2003

Biological Chemistry

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“…LR was first identified as a 67 kD protein which binds laminin with high affinity [38] and is expressed in a wide variety of cells [22]. Although LR has no obvious signal peptide and precursor of LR remained in cytoplasm as a component of the translational machinery [39], cell surface association of mature LR has been well documented [40,41].…”

Section: Discussionmentioning

confidence: 99%

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Amano

Kwak

et al. 2005

Cell Res

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The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has long been implicated to play an important role in extracellular matrix (ECM) remodeling and cell fate determination during normal and pathological processes. However, like other MMPs, the molecular basis of ST3 function in vivo remains unclear due to the lack of information on its physiological substrates. Furthermore, ST3 has only weak activities toward all tested ECM proteins. Using thyroid hormone-dependent Xenopus laevis metamorphosis as a model, we demonstrated previously that ST3 is important for apoptosis and tissue morphogenesis during intestinal remodeling. Here, we used yeast two-hybrid screen with mRNAs from metamorphosing tadpoles to identify potential substrate of ST3 during development. We thus isolated the 37 kd laminin receptor precursor (LR). We showed that LR binds to ST3 in vitro and can be cleaved by ST3 at two sites, distinct from where other MMPs cleave. Through peptide sequencing, we determined that the two cleavage sites are in the extracellular domain between the transmembrane domain and laminin binding sequence. Furthermore, we demonstrated that these cleavage sites are conserved in human LR. These results together with high levels of human LR and ST3 expression in carcinomas suggest that LR is a likely in vivo substrate of ST3 and that its cleavage by ST3 may alter cell-extracellular matrix interaction, thus, playing a role in mediating the effects of ST3 on cell fate and behavior observed during development and pathogenesis.

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“…[1][2][3][4] Eventually, it was demonstrated that the protein was expressed on a number of different tumor types. Several studies concluded that the protein was over-expressed at both the protein and mRNA levels on malignant tissues and cells as compared to their normal counterparts (reviewed in 5).…”

Section: Introductionmentioning

confidence: 99%

Monoclonal antibodies specific for oncofetal antigen – immature laminin receptor protein: Effects on tumor growth and spread in two murine models

McClintock

Warner

Ali

et al. 2015

Cancer Biology & Therapy

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The oncofetal antigen -immature laminin receptor protein (OFA/iLRP) has been linked to metastatic tumor spread for several years. The present study, in which 2 highly-specific, high-affinity OFA/iLRP-reactive mouse monoclonal antibodies were examined for ability to suppress tumor cell growth and metastatic spread in the A20 B-cell leukemia model and the B16 melanoma model, provides the first direct evidence that targeting OFA/iLRP with exogenous antibodies can have therapeutic benefit. While the antibodies were modestly effective at preventing tumor growth at the primary injection site, both antibodies strongly suppressed end-organ tumor formation following intravenous tumor cell injection. Capacity of anti-OFA/iLRP antibodies to suppress tumor spread through the blood in the leukemia model suggests their use as a therapy for individuals with leukemic disease (either for patients in remission or even as part of an induction therapy). The results also suggest use against metastatic spread with solid tumors.

show abstract

Isolation of a tumor cell laminin receptor

Cited by 393 publications

References 9 publications

Different Isoforms of the Non-Integrin Laminin Receptor Are Present in Mouse Brain and Bind PrP

Different Isoforms of the Non-Integrin Laminin Receptor Are Present in Mouse Brain and Bind PrP

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Monoclonal antibodies specific for oncofetal antigen – immature laminin receptor protein: Effects on tumor growth and spread in two murine models

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